Výsledky vyhledávání

Overexpression of mitogen-activated protein kinase kinase (MAPKK) and its mutants in NIH 3T3 cells. Evidence that MAPKK involvement in cellular proliferation is regulated by phosphorylation of serine residues in its kinase subdomains VII and VIII

Autor: Grażyna Dobrowolska, Jean S. Campbell, Edmond H. Fischer, Rony Seger, E G Krebs, Dalia Seger, Hagit Eldar-Finkelman, Erlynda Munar, Amy M. Jensen, Alfred A. Reszka

Publikováno v: Journal of Biological Chemistry. 269:25699-25709

Mitogen-activated protein kinase kinase (MAPKK) is a dual specificity protein kinase that exhibits a high degree of specificity toward its downstream target, mitogen-activated protein kinase (MAPK). In this study, we used stable overexpression of MAP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c3fd53137ccb9d2b058dacff20011c27
https://doi.org/10.1016/s0021-9258(18)47305-x

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Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis

Autor: Fred J. Lozeman, Bernhard Lüscher, David W. Litchfield, Robert N. Eisenman, E G Krebs

Publikováno v: Journal of Biological Chemistry. 267:13943-13951

In human epidermal carcinoma A431 cells, the beta subunit of casein kinase II is phosphorylated at an autophosphorylation site and at serine 209 which can be phosphorylated in vitro by p34cdc2 (Litchfield, D. W., Lozeman, F. J., Cicirelli, M. F., Har

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::67e83bdd537464aeffc50b9c754c8876
https://doi.org/10.1016/s0021-9258(19)49661-0

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Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2

Autor: C.J. Piening, David W. Litchfield, E G Krebs, Maria Harrylock, Fred J. Lozeman, M.F. Cicirelli, Lowell H. Ericsson

Publikováno v: Journal of Biological Chemistry. 266:20380-20389

To examine the phosphorylation of casein kinase II in cells, the enzyme was isolated by immunoprecipitation from metabolically labeled human epidermal carcinoma A431 cells using polyclonal antipeptide antibodies specific for either the alpha subunit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8cebc5957e7c9efa67a08156eacc55ed
https://doi.org/10.1016/s0021-9258(18)54934-6

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Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin

Autor: R H Clark, E G Krebs, Daniel R. Storm, E D Apel, David W. Litchfield

Publikováno v: Journal of Biological Chemistry. 266:10544-10551

Neuromodulin (P-57, GAP-43, B-50, F-1) is a neurospecific calmodulin-binding protein believed to play a role in regulation of neurite outgrowth and neuroplasticity. Neuromodulin is phosphorylated by protein kinase C, and this phosphorylation prevents

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f8ccec37803e4a8ced7fddba13e284d6
https://doi.org/10.1016/s0021-9258(18)99258-6

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Multiple components in an epidermal growth factor-stimulated protein kinase cascade

Autor: Curtis D. Diltz, E G Krebs, Nicholas K. Tonks, Natalie G. Ahn, Rony Seger, Rebecca L. Bratlien

Publikováno v: Journal of Biological Chemistry. 266:4220-4227

Epidermal growth factor stimulates the activity of several cytosolic serine/threonine protein kinases in quiescent Swiss 3T3 cells. Two of these, which use myelin basic protein (MBP) as substrate, act as kinase kinases in that they are able to activa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b6112e86f210e5c44abe06bb9b8b7dc1
https://doi.org/10.1016/s0021-9258(20)64310-1

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Activation of messenger-independent protein kinases in wild-type and phorbol ester-resistant EL4 thymoma cells

Autor: E G Krebs, Timothy A.J. Haystead, Karen A. Licciardi, Kathryn E. Meier

Publikováno v: Journal of Biological Chemistry. 266:1914-1920

Phorbol esters, acting via activation of the protein kinase C family of protein serine/threonine kinases, are able to exert profound effects on various cellular functions. In this study, we used the EL4 thymoma cell line to study the potential role o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::175aa387d58a00e5095d1c4bd771e30f
https://doi.org/10.1016/s0021-9258(18)52380-2

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Okadaic acid mimics the action of insulin in stimulating protein kinase activity in isolated adipocytes. The role of protein phosphatase 2a in attenuation of the signal

Autor: J E Weiel, Edmond H. Fischer, Timothy A.J. Haystead, E G Krebs, Y. Tsukitani, David W. Litchfield

Publikováno v: Journal of Biological Chemistry. 265:16571-16580

Treatment of adipocytes with okadaic acid (a specific inhibitor of type 1 and 2a protein phosphatases) resulted in a rapid 8-10-fold stimulation of cell extract myelin basic protein (MBP) kinase activity (t1/2 = 10 min) and kinase activity toward a s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2cf7e49924e6ec87bd455e2b14df7b67
https://doi.org/10.1016/s0021-9258(17)46261-2

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